(data stored in SCRATCH zone)

SWISSPROT: Q6BLX1_DEBHA

ID   Q6BLX1_DEBHA            Unreviewed;       414 AA.
AC   Q6BLX1;
DT   16-AUG-2004, integrated into UniProtKB/TrEMBL.
DT   04-NOV-2008, sequence version 2.
DT   08-MAY-2019, entry version 77.
DE   RecName: Full=Dipeptidase {ECO:0000256|RuleBase:RU341113};
DE            EC=3.4.13.19 {ECO:0000256|RuleBase:RU341113};
GN   OrderedLocusNames=DEHA2F10010g {ECO:0000313|EMBL:CAG89141.2};
OS   Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / JCM 1990 / NBRC
OS   0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX   NCBI_TaxID=284592 {ECO:0000313|EMBL:CAG89141.2, ECO:0000313|Proteomes:UP000000599};
RN   [1] {ECO:0000313|EMBL:CAG89141.2, ECO:0000313|Proteomes:UP000000599}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 36239 / CBS 767 / JCM 1990 / NBRC 0083 / IGC 2968
RC   {ECO:0000313|Proteomes:UP000000599};
RX   PubMed=15229592; DOI=10.1038/nature02579;
RG   Genolevures;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S.,
RA   Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E.,
RA   Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V.,
RA   Barnay S., Blanchin S., Beckerich J.M., Beyne E., Bleykasten C.,
RA   Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A.,
RA   Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A.,
RA   Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R.,
RA   Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H.,
RA   Nicaud J.M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O.,
RA   Pellenz S., Potier S., Richard G.F., Straub M.L., Suleau A.,
RA   Swennene D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B.,
RA   Zeniou-Meyer M., Zivanovic I., Bolotin-Fukuhara M., Thierry A.,
RA   Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA   Wincker P., Souciet J.L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of dipeptides.; EC=3.4.13.19;
CC         Evidence={ECO:0000256|RuleBase:RU341113};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|RuleBase:RU341113};
CC   -!- SIMILARITY: Belongs to the metallo-dependent hydrolases
CC       superfamily. Peptidase M19 family.
CC       {ECO:0000256|RuleBase:RU341113}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   EMBL; CR382138; CAG89141.2; -; Genomic_DNA.
DR   RefSeq; XP_460800.2; XM_460800.1.
DR   STRING; 4959.XP_460800.2; -.
DR   EnsemblFungi; CAG89141; CAG89141; DEHA2F10010g.
DR   GeneID; 2904212; -.
DR   KEGG; dha:DEHA2F10010g; -.
DR   HOGENOM; HOG000072016; -.
DR   InParanoid; Q6BLX1; -.
DR   KO; K01273; -.
DR   OMA; ALCDHSR; -.
DR   OrthoDB; 1272387at2759; -.
DR   Proteomes; UP000000599; Chromosome F.
DR   GO; GO:0016805; F:dipeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   CDD; cd01301; rDP_like; 1.
DR   InterPro; IPR032466; Metal_Hydrolase.
DR   InterPro; IPR008257; Pept_M19.
DR   PANTHER; PTHR10443; PTHR10443; 1.
DR   Pfam; PF01244; Peptidase_M19; 1.
DR   SUPFAM; SSF51556; SSF51556; 1.
DR   PROSITE; PS51365; RENAL_DIPEPTIDASE_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q6BLX1.
DR   SWISS-2DPAGE; Q6BLX1.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000599};
KW   Dipeptidase {ECO:0000256|RuleBase:RU341113};
KW   Hydrolase {ECO:0000256|RuleBase:RU341113};
KW   Metal-binding {ECO:0000256|RuleBase:RU341113};
KW   Metalloprotease {ECO:0000256|RuleBase:RU341113};
KW   Protease {ECO:0000256|RuleBase:RU341113};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000599};
KW   Zinc {ECO:0000256|RuleBase:RU341113}.
SQ   SEQUENCE   414 AA;  47098 MW;  1A89F47811339F7D CRC64;
     MVGKHIDEDL IKRFETLSSE TPIVDTHNDF PYLLRVQLHN EFETVNRFKF DDKLQSHTDL
     GKFRRGRVGL QFFSCFIECK DDDYLYQDFN NPNSAVRDTM EQIDVVTRLV SSYSEDLEMV
     SMSSQVMDVY SNGKIAISMG VEGLHQVDSS LSVLRKYYEL GVRYITLTHN CDNPFATAAS
     SVVAGLPDNG LSDFGRSCVL EMNRIGMMVD LSHVSYKTML DALEITKAPV MFSHSSAYTM
     TPNERNVRDD VLLRLKENNG VICINFFPSF ISPHSDENAI IDDAVNHIKH VVELIGWEHV
     GLGSDFDGIP EGPKGLEDVS KYPDLIIKVM GNLNASDSQI RLLMGDNVLR VWNENEKVAK
     SLQIAGTQLV NENWQKRDWS FFDYARSFRE LYPGAYEEKT NTYKDASLDL TKEK
//

If you have problems or comments...

PBIL Back to PBIL home page